Search results for "Two-hybrid"

showing 10 items of 33 documents

Usher syndrome and Leber congenital amaurosis are molecularly linked via a novel isoform of the centrosomal ninein-like protein.

2009

Contains fulltext : 80984.pdf (Publisher’s version ) (Closed access) Usher syndrome (USH) and Leber congenital amaurosis (LCA) are autosomal recessive disorders resulting in syndromic and non-syndromic forms of blindness. In order to gain insight into the pathogenic mechanisms underlying retinal degeneration, we searched for interacting proteins of USH2A isoform B (USH2A(isoB)) and the LCA5-encoded protein lebercilin. We identified a novel isoform of the centrosomal ninein-like protein, hereby named Nlp isoform B (Nlp(isoB)), as a common interactor. Although we identified the capacity of this protein to bind calcium with one of its three EF-hand domains, the interacton with USH2A(isoB) did …

Gene isoformRetinal degenerationCandidate geneGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeMolecular Sequence DataOptic Atrophy Hereditary LeberBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]CiliopathiesRetinaCell LineMiceCiliogenesisTwo-Hybrid System TechniquesGeneticsmedicineotorhinolaryngologic diseasesAnimalsHumansProtein IsoformsPhotoreceptor CellsAmino Acid SequenceNuclear proteinRats WistarEye ProteinsMolecular BiologyGenetics (clinical)GeneticsExtracellular Matrix ProteinsCiliumNuclear ProteinsGeneral MedicineArticlesmedicine.diseaseRatsMice Inbred C57BLMicrotubule-Associated ProteinsSequence AlignmentUsher SyndromesFunctional Neurogenomics [DCN 2]Protein BindingHuman Molecular Genetics
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Association of Whirlin with Cav1.3 (α1D) Channels in Photoreceptors, Defining a Novel Member of the Usher Protein Network

2010

Contains fulltext : 88383.pdf (Publisher’s version ) (Closed access) PURPOSE: Usher syndrome is the most common form of hereditary deaf-blindness. It is both clinically and genetically heterogeneous. The USH2D protein whirlin interacts via its PDZ domains with other Usher-associated proteins containing a C-terminal type I PDZ-binding motif. These proteins co-localize with whirlin at the region of the connecting cilium and at the synapse of photoreceptor cells. This study was undertaken to identify novel, Usher syndrome-associated, interacting partners of whirlin and thereby obtain more insights into the function of whirlin. METHODS: The database of ciliary proteins was searched for proteins…

Genetics and epigenetic pathways of disease [NCMLS 6]Calcium Channels L-TypeUsher syndromeProtein subunitImmunoelectron microscopyBlotting WesternPDZ domainRetinaCav1.3MiceTwo-Hybrid System TechniquesChlorocebus aethiopsmedicineAnimalsInner earRNA MessengerRats WistarDatabases ProteinMicroscopy ImmunoelectronPhotoreceptor Connecting CiliumIn Situ HybridizationRenal disorder [IGMD 9]RetinaVoltage-dependent calcium channelbiologyComputational BiologyMembrane Proteinsmedicine.diseaseeye diseasesRatsCell biologyMice Inbred C57BLmedicine.anatomical_structureCOS Cellsbiology.proteinsense organsFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateInvestigative Opthalmology & Visual Science
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Interaction of syntenin-1 and the NG2 proteoglycan in migratory oligodendrocyte precursor cells.

2008

Migration of oligodendrocyte precursors along axons is a necessary prerequisite for myelination, but little is known about underlying mechanisms. NG2 is a large membrane proteoglycan implicated in oligodendrocyte migration. Here we show that a PDZ domain protein termed syntenin-1 interacts with NG2 and that syntenin-1 is necessary for normal rates of migration. The association of syntenin-1 with NG2, identified in a yeast two-hybrid screen, was confirmed by colocalization of both proteins within processes of oligodendroglial precursor cells and by coimmunoprecipitation from cell extracts. Syntenin-1 also colocalizes with NG2 in "co-capping" assays, demonstrating a lateral association of bot…

ImmunoprecipitationSynteninsCellPDZ domainAmino Acid MotifsBiologyBiochemistryMiceCell MovementPrecursor cellTwo-Hybrid System TechniquesmedicineAnimalsHumansAntigensRNA Small InterferingMolecular BiologyCells CulturedNG2 proteoglycanColocalizationCell DifferentiationCell BiologyMolecular biologyOligodendrocyteCell biologyOligodendrogliamedicine.anatomical_structurenervous systemProteoglycanbiology.proteinProteoglycansNeurogliaProtein BindingThe Journal of biological chemistry
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Synthesis and biological evaluation of cycloalkylidene carboxylic acids as novel effectors of Ras/Raf interaction.

2002

The protooncogenes Ras and Raf play important roles in signal transduction pathways regulated by mitogen-activated protein kinases. Mutations of Ras that arrest the protein in its active state are frequently implicated in tumor formation. We used Ras and Raf proteins in the yeast two-hybrid system to search for natural or synthesized substances capable of modulating Ras/Raf interaction by specifically binding to one of the interacting partners. We found that cycloalkylidene carboxylic acids enhanced Ras/Raf interaction by acting on the cysteine-rich domain of Raf. Several analogues of the active substance 2-cyclohexylidene propanoic acid were synthesized and the importance of the semicyclic…

MAPK/ERK pathwayMagnetic Resonance SpectroscopyCarboxylic acidSaccharomyces cerevisiaeAmino Acid MotifsCarboxylic AcidsAnti-apoptotic Ras signalling cascadeTwo-Hybrid System TechniquesDrug DiscoveryHumansHRASProtein kinase Achemistry.chemical_classificationbiologyChemistryKinasebiology.organism_classificationProtein Structure TertiaryProto-Oncogene Proteins c-rafBiochemistryModels ChemicalMutationMutagenesis Site-Directedras ProteinsMolecular MedicineSignal transductionPlasmidsProtein BindingJournal of medicinal chemistry
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Cloning of Rac and Rho-GDI from tobacco using an heterologous two-hybrid screen.

2000

International audience; To examine whether molecular similarities exist between the animal and plant Rho GTPase signaling pathways, we have developed a heterologous two-hybrid screening method. By this technique, we have cloned a cDNA encoding a tobacco Rac-like protein able to interact with a mammalian Rho-GDI. In a second screen this tobacco Rac was used as a bait and a tobacco homologue of Rho-GDI was identified. These results show that some components of the animal and plant Rac signaling pathways are similar enough to allow their interaction in an heterologous approach. Moreover these data suggest a similar regulation of Rho GTPases in animals and plants.

MESH: Signal TransductionMESH: Plants ToxicMESH: Sequence Homology Amino Acid[SDV]Life Sciences [q-bio]Molecular Sequence DataMESH: rac GTP-Binding ProteinsMESH: Amino Acid SequenceMESH: Two-Hybrid System Techniques[SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunityMESH: Sequence AnalysisGene Expression Regulation PlantTwo-Hybrid System TechniquesTobacco[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumansrho-Specific Guanine Nucleotide Dissociation InhibitorsMESH: Guanine Nucleotide Dissociation InhibitorsMESH: Cloning Molecular[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMESH: rho-Specific Guanine Nucleotide Dissociation InhibitorsCloning MolecularMESH: Gene Expression Regulation PlantMESH: Tobacco[SDV.IMM.II] Life Sciences [q-bio]/Immunology/Innate immunityComputingMilieux_MISCELLANEOUSGuanine Nucleotide Dissociation InhibitorsPlant ProteinsMESH: HumansMESH: Molecular Sequence DataSequence Homology Amino AcidMESH: Plant ProteinsGENETIQUErac GTP-Binding Proteins[SDV] Life Sciences [q-bio]Plants ToxicSequence AnalysisSignal Transduction
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A New Nuclear Function of the Entamoeba histolytica Glycolytic Enzyme Enolase: The Metabolic Regulation of Cytosine-5 Methyltransferase 2 (Dnmt2) Act…

2009

Cytosine-5 methyltransferases of the Dnmt2 family function as DNA and tRNA methyltransferases. Insight into the role and biological significance of Dnmt2 is greatly hampered by a lack of knowledge about its protein interactions. In this report, we address the subject of protein interaction by identifying enolase through a yeast two-hybrid screen as a Dnmt2-binding protein. Enolase, which is known to catalyze the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), was shown to have both a cytoplasmatic and a nuclear localization in the parasite Entamoeba histolytica. We discovered that enolase acts as a Dnmt2 inhibitor. This unexpected inhibitory activity was antagonized by…

MethyltransferaseQH301-705.5ImmunologyEnolaseProtozoan ProteinsPolymerase Chain ReactionMicrobiologyEntamoeba histolyticaTwo-Hybrid System TechniquesGenetics and Genomics/EpigeneticsVirologyGeneticsImmunoprecipitationDNA (Cytosine-5-)-MethyltransferasesMicrobiology/ParasitologyBiology (General)Molecular BiologyMolecular Biology/DNA MethylationCell Nucleuschemistry.chemical_classificationbiologyEntamoeba histolyticaInfectious Diseases/Protozoal InfectionsMethylationRC581-607biology.organism_classificationTRNA MethyltransferasesEnolase 2EnzymechemistryBiochemistryPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationParasitologyImmunologic diseases. AllergyNuclear localization sequenceResearch ArticlePLoS Pathogens
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MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes

2002

Defects of the myosin VIIa motor protein cause deafness and retinal anomalies in humans and mice. We report on the identification of a novel myosin-VIIa-interacting protein that we have named MyRIP (myosin-VIIa- and Rab-interacting protein), since it also binds to Rab27A in a GTP-dependent manner. In the retinal pigment epithelium cells, MyRIP, myosin VIIa and Rab27A are associated with melanosomes. In transfected PC12 cells, overexpression of MyRIP was shown to interfere with the myosin VIIa tail localization. We propose that a molecular complex composed of Rab27A, MyRIP and myosin VIIa bridges retinal melanosomes to the actin cytoskeleton and thereby mediates the local trafficking of thes…

Molecular Sequence Datamacromolecular substancesMyosinsBiologyBiochemistryRetinarab27 GTP-Binding ProteinsMotor proteinMicechemistry.chemical_compoundTwo-Hybrid System Techniquesotorhinolaryngologic diseasesGeneticsmedicineAnimalsHumansAmino Acid SequenceRAB27Molecular BiologyGene LibraryMelanosomesRetinal pigment epitheliumScientific ReportsDyneinsRetinalActin cytoskeletonCell biologymedicine.anatomical_structurechemistryOrgan Specificityrab GTP-Binding ProteinsMelanosome transportMyosin VIIaMelanophilinsense organsRabSequence Alignmentcirculatory and respiratory physiologyEMBO reports
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Protein kinase inhibitor β enhances the constitutive activity of G-protein-coupled zinc receptor GPR39.

2014

GPR39 is a G-protein-coupled zinc receptor that protects against diverse effectors of cell death. Its protective activity is mediated via constitutive activation of Gα13 and the RhoA pathway, leading to increased SRE (serum-response element)-dependent transcription; the zinc-dependent immediate activation of GPR39 involves Gq-mediated increases in cytosolic Ca2+ and Gs coupling leading to increased cAMP levels. We used the cytosolic and soluble C-terminus of GPR39 in a Y2H (yeast-2-hybrid) screen for interacting proteins, thus identifying PKIB (protein kinase A inhibitor β). Co-expression of GPR39 with PKIB increased the protective activity of GPR39 via the constitutive, but not the ligand-…

RHOAmedicine.drug_classG proteinCHO CellsBiochemistryCell LineReceptors G-Protein-CoupledMiceCricetulusTwo-Hybrid System TechniquesmedicineAnimalsHumansProtein kinase AReceptorMolecular BiologyProtein Kinase InhibitorsbiologyEffectorCell MembraneIntracellular Signaling Peptides and ProteinsCell BiologyProtein kinase inhibitorCyclic AMP-Dependent Protein KinasesProtein Kinase A InhibitorCytosolZincBiochemistrybiology.proteinHeLa CellsThe Biochemical journal
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Bromodomain factor 1 (Bdf1) protein interacts with histones

2001

AbstractUsing a yeast two-hybrid assay we detected an interaction between the N-terminal region of histone H4 (amino acids 1–59) and a fragment of the bromodomain factor 1 protein (Bdf1p) (amino acids 304–571) that includes one of the two bromodomains of this protein. No interaction was observed using fragments of histone H4 sequence smaller than the first 59 amino acids. Recombinant Bdf1p (rBdf1p) demonstrates binding affinity for histones H4 and H3 but not H2A and H2B in vitro. Moreover, rBdf1p is able to bind histones H3 and H4 having different degrees of acetylation. Finally, we have not detected histone acetyltransferase activity associated with Bdf1p.

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsBiophysicsBromodomainTwo-hybridBiochemistryFungal ProteinsHistonesHistone H4SaccharomycesAcetyltransferasesGenes ReporterStructural BiologyTwo-Hybrid System TechniquesHistone methylationHistone H2AGeneticsHistone acetyltransferase activityHistone octamerMolecular BiologyHistone AcetyltransferasesBromodomain factor 1 proteinbiologyChemistryCell BiologyHistone acetyltransferasePeptide FragmentsChromatinBromodomainHistoneBiochemistryPCAFbiology.proteinHistone acetyltransferaseProtein BindingTranscription FactorsFEBS Letters
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Isolation of the silicatein-α interactor silintaphin-2 by a novel solid-phase pull-down assay.

2011

The skeleton of siliceous sponges consists of amorphous biogenous silica (biosilica). Biosilica formation is driven enzymatically by means of silicatein(s). During this unique process of enzymatic polycondensation, skeletal elements (spicules) that enfold a central proteinaceous structure (axial filament), mainly comprising silicatein, are formed. However, only the concerted action of silicatein and other proteins can explain the genetically controlled diversity of spicular morphotypes, from simple rods with pointed ends to intricate structures with up to six rays. With the scaffold protein silintaphin-1, a first silicatein interactor that facilitates the formation of the axial filament and…

Scaffold proteinSpiculeImmunoprecipitationMolecular Sequence DataNanotechnologyBiologyFlagellumBiochemistry03 medical and health sciencesSponge spiculePhase (matter)Two-Hybrid System TechniquesProtein Interaction MappingAnimalsInteractorAmino Acid Sequence030304 developmental biology0303 health sciences030302 biochemistry & molecular biologySilicon DioxideCathepsinsYeastProtein TransportSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationBiophysicsAutoradiographyCalciumSuberitesProtein BindingBiochemistry
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